accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q3TIX9
|
SNUT2_MOUSE
|
Inactive ubiquitin-specific peptidase 39
|
Mus
|
MSSRSKRQSHGSTRGKRESESRGSSGRIKKERDREKEPEAASSRGSPVRVKREAEPAAREVPAPALPVVRVKREREADEDSEPEREVRAKNGRVDSEDRRSRHCPYLDTINRSVLDFDFEKLCSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSSLEDITYVLKPTFTKQQIANLDKQAKLSRAYDGTTYLPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRPPGDIMFLLVQRFGELMRKLWNPRNFKAHVSPHEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIVNDVFQGSMRIFTKKLPHPDLPAEEKEQLLHNDEYQETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGITEKEYKTYKENFLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYLSEEVQAVHKNTTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWKRRDNDETNQQGA
|
Plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the precatalytic spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in cytokinesis and in the spindle checkpoint. Does not have ubiquitin-specific peptidase activity.
|
Q3TIX9
|
Q8K304
|
TM129_MOUSE
|
RING-type E3 ubiquitin transferase TM129
|
Mus
|
MDSPEVTFTLAYLVFAVCFVFTPNEFYSAGLTVQNLLSGWLGSEDAAFVPYHLRRTSATLLCHSLLPLGYYMGMCFAASEKQLYSPGQAPEAWQLFLLLAVTLPLLSCTLIYYWSWDRWTRHPLAQTLALYALPQSGWQAVASSINTEFRRIDKFATGAPGARVIVTDTWVMKVTTYRVHVAQQQDVHLTVTESRQHDLSPDSNLPVQLLTIRVASTSPGTQPFDIRLNSSEYGELCEKLHAPIRSAANVVIRQSLGDLFLETFASHVEVNPAYSVPSNQELEPCIGCMQTRASVKLVKTCQEPAVGECQQCYCRPMWCLTCMGKWFASRQDPQRPDTWLASRVPCPTCRARFCILDVCCVR
|
E3 ubiquitin-protein ligase involved in ER-associated protein degradation, preferentially associates with the E2 enzyme UBE2J2. Exploited by viral US11 proteins to mediate HLA class I proteins degradation.
|
Q8K304
|
B7KI14
|
RL13_GLOC7
|
50S ribosomal protein L13
|
Gloeothece citriformis
|
MEKTTLPNLETLDKQWYVIDAAGQRLGRLASEIAMILRGKNKPTYTPHLDTGDFVIVINAEKVIVTGKKSQQKVYHRHSGRPGGMKVETFEKLQARLPERIVEKAVKGMLPKNSLGRQLFTKLKVYSGSNHPHQAQKPETLTINTIPGGNN
|
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
|
B7KI14
|
Q59199
|
G3P_BACFR
|
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
|
Bacteroides
|
MIKVGINGFGRIGRMVFRAAVKNFGNDIQIVGINDLLDAEYLAYMLKYDSVHGRFEGEVAVEDGALIVNGNKIRLTAEMDPANLKWNEVDADVVVESTGFFLTDETARKHIQAGAKKVIMSAPSKDSTPMFVYGVNHTSYAGQDIISNASCTTNCLAPIAKVLNDKFGIVKGLMTTVHAATATQKTVDGPSKKDWRGGRGILENIIPSSTGAAKAVGKVLPVLNGKLTGMAFRVPTSDVSVVDLTVVLEKAATMAEINAAMKEASEGELKGILGYTEDAVVSTDFRGCANTSIYDSKAGISLDSNFAKVVSWYDNEWGYSNKVCEMARVIAAK
|
Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
|
Q59199
|
Q8BIW9
|
CTF18_MOUSE
|
Chromosome transmission fidelity protein 18 homolog
|
Mus
|
MEDYEEDLYGVEDDFQNQFAAELEVLAELEGTRDQAPPGTLQTPASRPPLTFEEAIAGGDTVPRPCPAGSPGNVNRNTRKNVRRDQPAPSSPMVKRPRLDVVKKLNFEPDMEELLYPDSPPGDITPPPSPEVFPEMLDAGYSDANADKDLMQTLPSPRNRNPVLRRPPILEDYINVTSTSGERAFLVLRADLIGPGVQNPLLDVHWRGCGQLDLLGVPFASLKEQVDSKRRQQLLEDAQQLSDTLHSLRSEGEEAVLEGPPAEEPAPGQNTAQHCLWVDEFAPQHYTELLSDDFTNRCLLKWLKLWDLVVFGRERPARKPRPGVETTRVGKEATAPGKWKSHEQALEEMLEAELDPSQRPRQKVALLCGPPGLGKTTLAHVVARHAGYCVVEMNASDDRSPEAFRTRIEAATQMESVLGVGGRPNCLVIDEIDGAPTAAINVLLGILNRKGPQEADQGGTAVAAGGRRRRAEGGLLTRPIICICNDQFTPSLRQLKQQALLLHVPPTLPSRLVQRLQEISLQHGMRSDPGALVALCEKTDNDIRACINTLQFLYGRGRRELSVKAVQTTHVGLKDQRKGLFSVWQEVFQLPRTQRRIVGQDLMLPAHALLLSNGDKGSLTLASQRFYHILRVTTSAGEHEKVVQGLFDNFLRLRLRDSSLSTVCCALDWLAFDDLLEQAAHRGQSFQLLCYLPFVPAAFHVLFASSHVPRITFPSSQQEAQTRMSQTRNHIQTLVSGMAPTTRSRATPQALVLDTLCLLLDVLAPKLRPVSTQLYSAHEKQQLSCLVGTMLAYSLTYHQERTPDGQYLYKLEPNVEEVCRFPELPARKPLTYQAKQLIAREIEMEKMRRAEALAWARSGPQVDQGSSGPASLWTDSGEKGTRQPAPRNHEQRLEHIMKRATVQEQPERDFFGRVVIRKVAVPSREVEAPQKDADEWRMGVAVGRSEVWFRFNEGVSNAVRRSLYIRDLL
|
Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. Interacts with and stimulates DNA polymerase POLH. During DNA repair synthesis, involved in loading DNA polymerase POLE at the sites of local damage.
|
Q8BIW9
|
B8B8C5
|
ALFL9_ORYSI
|
PHD finger protein ALFIN-LIKE 9
|
Oryza sativa
|
MDAQYNPRTVEEVFRDFKGRRAGLVRALTADVEDFFRQCDPEKENLCLYGFPNEHWEVNLPAEEVPPELPEPALGINFARDGMQEKDWLSMVAVHSDAWLLSVAFYFGARFGFDKNDRKRLFGMINDLPTIFEVVSGKSKAKPPSANNHSNSKSKSSNKTKSSEPRAKQPKPQPQPPVKNEGREEEGGPDDEEGGGGGGGGREEEHGETLCGACGESYGADEFWICCDICEKWFHGKCVKITPAKAEHIKQYKCPSCSGGNGGGGGGSGNGKRARPS
|
Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
|
B8B8C5
|
O22229
|
TRXB3_ARATH
|
NADPH-dependent thioredoxin reductase C
|
Arabidopsis
|
MAASPKIGIGIASVSSPHRVSAASSALSPPPHLFFLTTTTTTRHGGSYLLRQPTRTRSSDSLRLRVSATANSPSSSSSGGEIIENVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGGVPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPEDVESLSVTTAPFTVQTSERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGASPLFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNTKGQMSGILLRRLDTGEETELEAKGLFYGIGHSPNSQLLEGQVELDSSGYVLVREGTSNTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYLTSNNLLVEFHQPQTEEAKKEFTQRDVQEKFDITLTKHKGQYALRKLYHESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYREFIEANK
|
Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for plastidial 2-Cys peroxiredoxins and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark. Required for chlorophyll biosynthesis and biogenesis of the photosynthetic apparatus. Activates aerobic cyclase which converts Mg-protoporhyrin monomethyl ester into protochlorophyllide. Involved in a light-dependent regulation of starch biosynthesis by redox activation of the ADP-glucose pyrophosphorylase (AGPase), a central enzyme of starch synthesis.
|
O22229
|
Q6MEB9
|
DTD_PARUW
|
Gly-tRNA(Ala) deacylase
|
Candidatus Protochlamydia
|
MKLVIQRVLQAQVYIDDNLFSAIGPGLMLLLGIHHQDNLEQILWSVDKLVHLRIFNDENGKMNRNVKECEGEILVVSQFTLYGNCLNGRRPDFIQAASPPIALSLYRQFIDELKKEAPHVKTGQFGAQMQVSLTNDGPVTFILESLDRRKA
|
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
|
Q6MEB9
|
C4K4D4
|
AROA_HAMD5
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Candidatus Hamiltonella
|
MSKSLNLEPIGKINGTVYLPGSKSISNRVLLLSALAAGKTRLTNFLDSDDTRYMLEALKALGVRYTVSKNGTCCEVEGVNGPLNTPHPIELMTGNAGTVMRFLTAVLSLGQSDVVLTGGARMKERPMDPLVDALRQGNAQITYLEKKNSPPLRLRGGFRGGNLTLRGNISSQFLTALLIMAPLAEQDTAIEVQGFLVSKPYVEMTLHLMRVFGISVTHKHYRTFNIKAHQKFKSPGHYRIEGDATAASYFLAAAAIKGGCVRVIGVGQKSIQGDVQFADVLQKMGAFIHWGEDYIECRPGRLKGIDMDMNSMPDAAMTLATTALFSEGPTRIQNIYNWRLKETDRLSAMSAELRKLGAQIKEGQDYIEIISPKNLKAAEIQTYNDHRIAMSFSLMALSDMPIRILNPRCTSKTFPDFFQKLAYLSGTV
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
C4K4D4
|
C5BCB6
|
PEPQ_EDWI9
|
Proline dipeptidase
|
Edwardsiella
|
MDTLASLYTKHLATLQQRARTILERHQLDGLLIHSGEPIARFLDDQDYPFKINPYFKAWVPVTQVPNCWLWIDGVNKPKLWFYSPLDYWHSVSPLPQAFWTEQVEMTAQRHADDIAALLPAARGNVAYIGPNAERARSLGIDEAHQNPQAVLNFLHYHRAYKSEYEQACMREAQKIAVDGHQAALEAFRAGMSEFDINLAYLSATGQGENDVPYDNIIALNRHAAVLHYTHLERRAPSEMHSFLIDAGAEFHGYAADLTRTYAANGQSDFAALVAEVNQAQQALIATLQTGVRYTDYNLQFHQRLAAILRHHHILTGISDEAAVAQGLTTPFLPHGLGHPLGLQVHDVAGFMQDELGTQMAAPDRYPYLRCTRIMEPGMVMTIEPGLYFIDTLLAPWLEGEFGQHFNRGRIDALRPYGGIRIEDNVIFHAHGVENMTRDLHLA
|
Splits dipeptides with a prolyl residue in the C-terminal position.
|
C5BCB6
|
Q4FNN3
|
YBEY_PELUB
|
Endoribonuclease YbeY
|
Candidatus Pelagibacter
|
MIKIDVVSECTLWSKKIKRNKTFFNSILKFFPKKYKFIGKKINLTILLSNNKNIKKLNKDFRNKNKPTDVLSFPFEKKFNPKKSNYLGDIVISYEFMNKPKNISILEFKQKVVKIFIHGFLHLLGHDHIKLKDFKKMIKEEDLIYKFIKTKVA
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q4FNN3
|
B9L7Y6
|
ATPG_NAUPA
|
F-ATPase gamma subunit
|
Nautilia
|
MATLKELKQKISSVKNTQKTTRAMKLVSTAKLKRAEEAIMRSREYARKIDEVMHEISAKLASVKDSIELRAFAKIENVEKVDVIVITADKGLCGGFNIQTIKQTIKLIEELKEKKVKIRLKVIGKKAIEYFKFVGIDMYEEVIGLSAAPNYEKAAELIQKSYEDFVNEEIDNIITIHNGYVNKLTQQVYVKELLPIEVDVNDSQEFLEVEPDNDYETILETLVKKYIEYSLYYALLDSLAAEHSARMQAMDAATNNAKEMVHQLTLEFNKARQEAVTRELIEIVTAIEAMKK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
B9L7Y6
|
P48454
|
PP2BC_HUMAN
|
Calmodulin-dependent calcineurin A subunit gamma isoform
|
Homo
|
MSGRRFHLSTTDRVIKAVPFPPTQRLTFKEVFENGKPKVDVLKNHLVKEGRLEEEVALKIINDGAAILRQEKTMIEVDAPITVCGDIHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTDYFTFKQECRIKYSEQVYDACMETFDCLPLAALLNQQFLCVHGGMSPEITSLDDIRKLDRFTEPPAFGPVCDLLWSDPSEDYGNEKTLEHYTHNTVRGCSYFYSYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQATGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELISDDEAEGSTTVRKEIIRNKIRAIGKMARVFSILRQESESVLTLKGLTPTGTLPLGVLSGGKQTIETATVEAVEAREAIRGFSLQHKIRSFEEARGLDRINERMPPRKDSIHAGGPMKSVTSAHSHAAHRSDQGKKAHS
|
Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32.
|
P48454
|
B9DV75
|
MRAY_STRU0
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Streptococcus
|
MFLTLIAGLISLLLTALIMPHFIKFYQMKKIGGQQMHEDVKQHLAKAGTPTMGGTVFLLVASFVSFLFAILFFSHGKSMGLITGILAIVLIYGFIGFLDDFLKIFKQINEGLTPIQKLSLQIVGGLIFYFLHVVPSGIDAINVFGFPVHLGLLYIFFVLFWVVGFSNAVNLTDGIDGLASISVVISLLTYSVIAIHQNQYDVLLLCGIMIGALLGFFIFNHKPAKVFMGDVGSLALGAMLAAISIALRQEWTLLVIGLVYVFETSSVMLQVSYFKYTKKKFGEGRRIFRMTPFHHHLELGGLSGKAERWSEWKVDAFLWSVGAVSSLIVLAILYL
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
B9DV75
|
Q8RII2
|
MNTP_FUSNN
|
Putative manganese efflux pump MntP
|
Fusobacterium
|
MSTISVLITALALSMDAMSLSIYQGIASTESQKKQNFLKIVLTFGIFQFAMALVGSLSGILFIHYISLYSKYVSFAIFLFLGLMMLKEALKKEEMEYDEKYLDFKTLIIMGIATSLDALLVGLTFSILPFYQTFLYTVEIGVITAIIAGLGFILGDKFGNILGQKSHFLGAALLIFISINILL
|
Probably functions as a manganese efflux pump.
|
Q8RII2
|
A3D2B0
|
NADK_SHEB5
|
ATP-dependent NAD kinase
|
Shewanella
|
MGINFDVSRPKARSSINMTTKFHTIGLIGKPHHQGTNQTLKRLHHWLTMQGFEVLVEERVAAELGPNIEAVDLLEIGARCDLAIVVGGDGNMLGAARVLARFDLGVIGVNRGNLGFLTDLPPDAFEEALAKVLDGEFDTEHRFLLEAEVYRHGMLKASNTAVNEAVLHPGKIAHMIEFEVYIDDQFMYSQRADGMIVSTPTGSTAYALSAGGAILTPNLQALILVPMFPHTLSCRPIVVDACSTIKMVVSPDNGENLEVSCDGHVHLAVLPGDEIIVRRSSERLRLIHPKGHNYFHVLRTKLGWGSKLF
|
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
|
A3D2B0
|
Q9AGU4
|
HUTU_PSESX
|
Imidazolonepropionate hydrolase
|
Pseudomonas
|
MTSTTPKSPAAFTRHRDGEIRAARGTQLTAKSWMTEAPLRMLMNNLDPQVAENPTELVVYGGIGRAARNWECYDKIVESLTNLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWATWEHFNELDAKGLAMYGQMTAGSWINIGSQGIVQGTYETFVEAGRQHYNGSLKGKWVLTAGLGGMGGAQPLAATLAGACSLNIECQQSRIDFRLATRYVDEQALDLDDALVRIAKYTAEGKAISIALCGNAAELLPEMVRRGVRPDMVTDQTSAHDPLNGYLPKGWTWEQYRDRAVTDPAAVVKAAKASMGEHVEAMLAFQKAGIPTFDYGNNIRQMAKEVGVENAFDFPGFVPAYIRPLFCRGVGPFRWVALSGDAEDIYKTDAKVKELIADDAHLHNWLDMARERISFQGLPARICWVGLGQRAKLGLAFNEMVRSGELKAPIVIGRDHLDSGSVSSPNRETESMKDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPATGVMRHADAGYDIAIDCANEQGLNLPMING
|
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
|
Q9AGU4
|
P86183
|
ETCHF_ENTFC
|
Enterocin-HF
|
Enterococcus
|
MEKLTVKEMSQVVGGKYYGNGVSCNKKGCSVDWGKAIGIIGNNAAANLTTGGKAGWKG
|
Bacteriocin.
|
P86183
|
Q07076
|
ANXA7_MOUSE
|
Synexin
|
Mus
|
MSYPGYPPTGYPPFPGYPPAGQESSFPTAGQYPYPSGFPPMGGGAYPPAPSGGYPGAGGYPAPGGYPAPGGYPGALSPGGPPAYPGGQGFGAPPGGAGFSGYPQPPAQSYGGGPAQVPVPGGFPGGQMPSQYPGGQAPYPSQPASMTQGTQGTILPASNFDAMRDAEILRKAMKGFGTDEQAIVDVVSNRSNDQRQQIKAAFKTMYGKDLIKDLKSELSGNMEELILALFMPSTYYDAWSLRKAMQGAGTQERVLIEILCTRTNQEIRDIVRCYQLEFGRDLEKDIRSDTSGHFERLLVSMCQGNRDERQSVNHQMAQEDAQRLYQAGEGRLGTDESCFNMILATRSFPQLKATMEAYSRMANRDLLSSVSREFSGYVESGLKTILQCALNRPAFFAERLYYSMKGAGTDDSTLVRIVVTRSEIDLVQIKQMFTQMYQKTLSTMIASDTSGDYRKLLLAIVGQ
|
Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.
|
Q07076
|
Q8HQS3
|
MATK_PINPT
|
Intron maturase
|
Pinus subgen. Pinus
|
MDEFHRCGKEDSFWQQCFLYPLFFQEDLYAISHDHYLDVSSSSRPMEHLSSNDQLSFLTVKRLIGQIRQQNHSIVLFVNCDPNPLADRKKSFYSESVLEALTLVLEVPFSIWSKYSVEGMNESKSFRSIHSIFPFLEDKFPHSNSILDARIPYSIHPEILVRTFRRWIRDAPSLHPLRSVLYEYRNSPDNLQRSIIVVPRVNTRFFLFLWNYYVCECESILFSRLKRSSHSRSLTHGSFPQRTHFHRKIKHIIIFSRRNSLKSIWSLKDPKIHYVRYGERPIIAIKGAHLLVKKCRYYLLIFRQFYFHLWSEPYRVCSHQLSKNCSSSPGYFLRVRMNPILVRTKMLDELFIADLITDEIDPIVPIVPIIGLLATEKFCDISGRPISKLSWTSLTDDDILDRFDQIWRNLFHYYSGSFDRDGLYRIKYILSLSCAKTLACKHKSTIRVVRKELGPELFKKSFSKEREFYSLRFSSKAAARSQRERIWHSDISQINPLANSWQKIQDLKIENLFDQ
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q8HQS3
|
P97846
|
CNTP1_RAT
|
p190
|
Rattus
|
MMSLRLFSILLAAVVSGAQGWGYYGCNEELVGPLYARSLGASSYYGLFTTARFARLHGISGWSPRIGDPNPWLQIDLMKKHRIRAVATQGAFNSWDWVTRYMLLYGDRVDSWTPFYQQGHNATFFGNVNDSAVVRHDLHYHFTARYIRIVPLAWNPRGKIGLRLGIYGCPYTSNILYFDGDDAISYRFQRGASQSLWDVFAFSFKTEEKDGLLLHTEGSQGDYVTLELQGAHLLLHMSLGSSPIQPRPGHTTVSAGGVLNDLSWHYVRVDRYGREANLTLDGYVHRFVLNGDFERLNLENEIFIGGLVGAARKNLAYRHNFRGCIENVIYNRINIAEMAVQRHSRITFEGNVAFRCLDPVPHPINFGGPHNFVQVPGFPRRGRLAVSFRFRTWDLTGLLLFSRLGDGLGHVELMLSEGQVNVSIAQTGRKKLQFAAGYRLNDGFWHEVNFVAQENHAVISIDDVEGAEVRVSYPLLIRTGTSYFFGGCPKPASRWGCHSNQTAFHGCMELLKVDGQLVNLTLVEFRKLGYFAEVLFDTCGITDRCSPNMCEHDGRCYQSWDDFICYCELTGYKGVTCHEPLYKESCEAYRLSGKYSGNYTIDPDGSGPLKPFVVYCDIRENRAWTVVRHDRLWTTRVTGSSMDRPFLGAIQYWNASWEEVSALANASQHCEQWIEFSCYNSRLLNTAGGYPYSFWIGRNEEQHFYWGGSQPGIQRCACGLDQSCIDPALHCNCDADQPQWRTDKGLLTFVDHLPVTQVVIGDTNRSSSEAQFFLRPLRCYGDRNSWNTISFRTGAALRFPPIRANHSLDVSFYFRTSAPSGVFLENMGGPFCQWRRPYVRVELNTSRDVVFAFDIGNGDENLTVHSDDFEFNDDEWHLVRAEINVKQARLRVDHRPWVLRPMPLQTYIWLEYDQPLYVGSAELKRRPFVGCLRAMRLNGVTLNLEGRANASEGTFPNCTGHCTHPRFPCFHGGRCVERYSYYTCDCDLTAFDGPYCNHDIGGFFETGTWMRYNLQSALRSAAQEFSHMLSRPVPGYEPGYIPGYDTPGYVPGYHGPGYRLPDYPRPGRPVPGYRGPVYNVTGEEVSFSFSTSSAPAVLLYVSSFVRDYMAVLIKEDGTLQLRYQLGTSPYVYQLTTRPVTDGQPHSVNITRVYRNLFIQVDYFPLTEQKFSLLVDSQLDSPKALYLGRVMETGVIDPEIQRYNTPGFSGCLSGVRFNNVAPLKTHFRTPRPMTAELAEAMRVQGELSESNCGAMPRLVSEVPPELDPWYLPPDFPYYHDDGWIAILLGFLVAFLLLGLVGMLVLFYLQNHRYKGSYHTNEPKATHDSHPGGKAPLPPSGPAQAPAPTPAPTQVPTPAPAPASGPGPRDQNLPQILEESRSE
|
Required, with CNTNAP2, for radial and longitudinal organization of myelinated axons. Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the paranodal region of the axo-glial junction. In association with contactin involved in the signaling between axons and myelinating glial cells.
|
P97846
|
Q04585
|
YDR09_YEAST
|
D-ribulokinase YDR109C
|
Saccharomyces
|
MKSRKRQNNMQNETREPAVLSSQETSISRISPQDPEAKFYVGVDVGTGSARACVIDQSGNMLSLAEKPIKREQLISNFITQSSREIWNAVCYCVRTVVEESGVDPERVRGIGFDATCSLVVVSATNFEEIAVGPDFTNNDQNIILWMDHRAMKETEEINSSGDKCLKYVGGQMSVEMEIPKIKWLKNNLEAGIFQDCKFFDLPDYLTFKATGKENRSFCSAVCKQGFLPVGVEGSDIGWSKEFLNSIGLSELTKNDFERLGGSLREKKNFLTAGECISPLDKKAACQLGLTEHCVVSSGIIDAYAGWVGTVAAKPESAVKGLAETENYKKDFNGAIGRLAAVAGTSTCHILLSKNPIFVHGVWGPYRDVLARGFWAAEGGQSCTGVLLDHLITTHPAFTELSHMANLAGVSKFEYLNKILETLVEKRKVRSVISLAKHLFFYGDYHGNRSPIADPNMRACIIGQSMDNSIEDLAVMYLSACEFISQQTRQIIEVMLKSGHEINAIFMSGGQCRNSLLMRLLADCTGLPIVIPRYVDAAVVFGSALLGAAASEDFDYTREKRTLKGQKSSQTKTERFNDSYSSIQKLSMEDRNSTNGFVSPHNLQLSTPSAPAKINNYSLPICTQQPLDKTSEESSKDASLTVGQESLGEGRYNGTSFLWKVMQELTGNARIVNPNEKTHPDRILLDTKYQIFLDMIETQRKYRRMVDKVEGSFSR
|
Catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. Postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
|
Q04585
|
Q6GQ76
|
CMTR1_XENLA
|
FtsJ methyltransferase domain-containing protein 2
|
Xenopus
|
MKRKSDSEQQPSVQCRKKKRIEELGLNLSSTSDDDTQYSNHGTQESSTSSTSSDSDNEEKRPVFGSGRNETLPDTLAEGSSSHYSMYNSVSQKLMAKMGFREGEGLGKFGQGRKEIVETSKQKGRRGLGMVLKGFEKELNINWRSEPEATAYEEVDWFPECTTDIPDSDELSDWMIVGKRKLIIDDETEFCRDNLLTSLLQCKSAFDELEGEEMRRARTRSNPYEMIRGVFFLNRAAMKMANIDHVFDYMFTNPKDSQGKPKLKDKESELLYFADVCAGPGGFSEYVLWRKKWHAKGFGMTLKGPNDFKLEDFYAAPSELFEPYYGEGGVDGDGDVTRPENITAFRNFILDNTDHKGVHFMMADGGFSVEGQENIQEILSKQLLLCQFLVGLHVIRTGGHFICKTFDLFTPFSVGLIYLLYCCFERVCLFKPLTSRPANSERYVVCRGLKEGIDDVRNYLFNVNRRLNHLRNSDQDVTLVVPLEVLRGDKQFNEYMVRSNESCCEVQIKALAKIHAFVQDSTLSESRQADIRRECLKLWGVPDQARVAPTNTDARTKFFQLIQSQNIEVFGYKPTPLTAKTLEKLIHVFDYRCMVCGSEPKFLLGLGRSQIYTWGGRSNERWTRLDLKTELPRDTLLSVEIVHELKGEGKAQRKISAIHVLDVLFLNGTDVRTQHFTQRIQLAEKFVRAVAKPSRPDMNPIRVKEVYRLEDIEKIFLRLDMKHIKSSGGYLRLSYTGRDDRHFVPCGLYIVKTINEPWSMAYSKSQKRKYFYNSKTKNSQFELPVESIAPFHTCYYERLFWEWGEGVQIHDSQRRDPDSDKLSKDAVLQFIQAHHPCMPSSLTEDR
|
S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway.
|
Q6GQ76
|
O04492
|
DRB1_ARATH
|
dsRNA-binding protein 1
|
Arabidopsis
|
MTSTDVSSGVSNCYVFKSRLQEYAQKYKLPTPVYEIVKEGPSHKSLFQSTVILDGVRYNSLPGFFNRKAAEQSAAEVALRELAKSSELSQCVSQPVHETGLCKNLLQEYAQKMNYAIPLYQCQKVETLGRVTQFTCTVEIGGIKYTGAATRTKKDAEISAGRTALLAIQSDTKNNLANYNTQLTVLPCEKKTIQAAIPLKETVKTLKARKAQFKKKAQKGKRTVAKNPEDIIIPPQPTDHCQNDQSEKIETTPNLEPSSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLEPSSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLESSSCMSGLKEAAFGSVETEASHA
|
Double-stranded RNA-binding protein involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis by assisting DICER-LIKE 1 (DCL1) in the accurate processing from primary miRNAs (pri-miRNAs) to miRNAs in the nucleus. Forms a complex with SERRATE (SE) and DCL1 to promote accurate processing of pri-miRNAs by DCL1. Binds and assist DCL1 for accurate processing of precursor miRNAs (pre-miRNA). Indirectly involved in the production of trans-acting small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in the production of their initiating miRNAs. Involved with argonaute 1 (AGO1) in the guide strand selection from miRNA duplexes, presumably by directional loading of the miRNA duplex (guide stand and passenger strand) onto the RNA-induced silencing complex (RISC) for passenger strand degradation. Does not participate in sense transgene-induced post-transcriptional gene silencing (S-PTGS). Involved in several plant development aspects and response to hormones through its role in miRNAs processing.
|
O04492
|
C6DKV3
|
OPGG_PECCP
|
Glucans biosynthesis protein G
|
Pectobacterium
|
MLDNKFGFKQRVASLRWLSAAIMLSVSAVPAWAFSIDDVAQQAEKLSQKGFEAPKSNLPAQFRDMKFADYQQIRFNNDKSYWNNVQTPFKLQFYHQGMYFDTPVKINEVTATTVDEIKYSPEYFDFGSVNHDAEAVKNLGFAGFKVLYPINKADKNDEIVSMLGASYFRVVGKGQIYGLSARGLAIDTALPSGEEFPRFREFWIERPKPNDKHLVIYALLDSPRAAGAYRFTVYPGRDSVVDVQAKVFLRDKVGKLGIAPLTSMYLFGPNQPSPTLNYRPALNDSNGLSIHAGNGEWIWRPLNNPKHLSVSTYAVENPKGFGLLQRGRDFTAYEDLDDRYDLRPSGWVEPKGEWGKGKVELVEIPTADETNDNIVAFWTPDVLPETGKPLDIKYRLHFTRDEDQLHSPNIAYVQQTRRSAGDVKQSNLIRQPDGTIAYIVDFVGPNLKELDESTPVASQVSIGDNGEIVENNVRYNPVTHGWRLTLRLRVKDAKQPTEMRAALVNGETTLTETWSNQLPANE
|
Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
|
C6DKV3
|
Q8DF02
|
DER_VIBVU
|
GTP-binding protein EngA
|
Vibrio
|
MIPVVALVGRPNVGKSTLFNRLTRSRDALVADFPGLTRDRKYGQAKVGEHDFIVIDTGGIDGSEEGVETKMAEQSLAAIREADVVLFMVDGRAGLTPSDEAIAAHLRKIEKATMLVVNKVDGIDADAASADFWQLGVDEMYQIAAAHGRGVTALIERALDPFFDNLLSANNEGEIEDLTDMEDEDAEQQEYSEEDAEESLKRLQDQPIKLAIIGRPNVGKSTLTNRILGEERVVVYDMPGTTRDSIYIPMERDGREYVLIDTAGVRRRGKVHETVEKFSVVKTLKAVEDANVVLLVIDARENISDQDLSLLGFALNAGRSIVLAVNKWDGLDNEVKENVKKELDRRLGFVDFARIHFISALHGTGVGHLFESVQEAYRSATTRVGTSVLTRIMKMATEDHQPPMVRGRRVKLKYAHAGGYNPPIVVIHGNQVRELPDSYKRYLMNYFRKSLDIMGTPIRIQFQNSDNPFENRVNKMTLSQERARKRMMSAVKNRKK
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
Q8DF02
|
A0A0E4AVP3
|
LEAM_RAMVA
|
Group 3 late-embryogenesis abundant protein, mitochondrial
|
Ramazzottius
|
MFLARNAGRAGYRGVVAYQQAASFSVSSAKAAGSRSSGGSDAGDYAREAAEHAKAGLKDLKNEASWKAKGVANQAAGAFERAKDTVKEGVHDMKRSGSRVFEQGQEEVEAGAQHAKAGYQSAKNAAQDTAATLKDKAGSAWNQAKHVVEDKGEDVVEAVKDTASKVWGKAKHVAEDVKENAQSPGGIADKASDVWSAAKDKAADVLSGAKHTAENLAHKAQAAIHDATASSGSQSQSQSQSQYRQGQQQGRQDQQQSKSQWGQTSPQSPDGFRPQAGQGPQGGKGPGQAGGRR
|
Mitochondrial heat soluble protein acting as a molecular shield in water-deficient condition.
|
A0A0E4AVP3
|
A5EWY9
|
IF2_DICNV
|
Translation initiation factor IF-2
|
Dichelobacter
|
MTVAELAKQLRISINRLLDVISEAGIVIHDVENDVLSPEQKVAIAGHMKQRKKQSATEKNAAKSDNKSDKNSKTGAKKTTNRRKTDARKSQSSEKKISPRELAQQLAEKKRLEQGNAQRENEEREYQEALAAEEKRQQQEEARKAKREQKEAEAIRAEEERLQMEAALQAQMQEQERIRQEKEAEEAKLNAEKELRKQQEREKRLAQEKAELERKRQEAIRDVELRESYEEEAETRFHIQSKDRNFGSKNDRSGKRAVKNGDDERSGERRNNARNNTRRRNNDNKKGKFEKPVAPISREVRIPETITVGDLAQKMSVKASELIKTMMKLGSMVTINQLLDQETAALIADEMGHRYVLLKENELEEQVMAQASENKMDVVVRAPVVTIMGHVDHGKTSLLDYIRHTRVVSGEAGGITQHIGAYRVTTERGVITFLDTPGHAAFTAMRARGANVTDIVVLVVAADDGVMPQTKEAIQHAKAANVPLIVAVNKMDKPEADPERVKSELSQEGVISEEWGGEHLFAYVSAKSGMGIDDLLEKILIQAEMLELTAPSSGVGKGVVVESRLDRGRGSVATVLVQSGVMKKGNVMLAGMEYGRIRAMLDEKGKELEEAGPSTPVEILGLSGTPNAGDDVIIVENERKAREIANFRQGKFKEIRIARQQKTKLENLFNNADGEISKVSLMIKADVQGSVEALADSLRELSTDEVAVNIIATGIGGITESDVQLALASSATIIAFNVRAEANAKKLIEEEGGDLRYYSIIYQAIDDVKAAMQGLLSPEIREEIIGLAEVRDVFRSSKFGAVAGCIVEDGLLKRHNPIRVLRNNVVIYEGELESLRRFKDDVNEVRAGTECGLGVKNYNDVRVGDQIECYERVEIERKL
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A5EWY9
|
P63013
|
PRRX1_MOUSE
|
Paired-related homeobox protein 1
|
Mus
|
MTSSYGHVLERQPALGGRLDSPGNLDTLQAKKNFSVSHLLDLEEAGDMVAAQADESVGEAGRSLLESPGLTSGSDTPQQDNDQLNSEEKKKRKQRRNRTTFNSSQLQALERVFERTHYPDAFVREDLARRVNLTEARVQVWFQNRRAKFRRNERAMLANKNASLLKSYSGDVTAVEQPIVPRPAPRPTDYLSWGTASPYSAMATYSATCANNSPAQGINMANSIANLRLKAKEYSLQRNQVPTVN
|
Acts as a transcriptional regulator of muscle creatine kinase (MCK) and so has a role in the establishment of diverse mesodermal muscle types. The protein binds to an A/T-rich element in the muscle creatine enhancer.
|
P63013
|
Q14K05
|
ATPE_FRAT1
|
F-ATPase epsilon subunit
|
Francisella
|
MTKKYLKVDVVSPLGSVFKGEADMVSLRGSAGEMGIAYGHTELLSTLPAGVVNVRKDQHTDVLYVSGGIVEVTPTRVTIMVDDMERAENLNQAEAEKARARAKEVLKNPDASKLDIEAANKRLKEADARLKALNSSNGLYYSKDD
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q14K05
|
P01065
|
IBB_VICSN
|
VAI
|
Vicia
|
GDDVKSACCDTCLCTRSQPPTCRCVDVGERCHSACNHCVCNYSNPPQCQCFDTHKFCYKACHSSEKEEVIKN
|
This inhibitor has two domains, each with separate antiprotease activity. 1 mole of inhibitor inhibits either 1 mole of trypsin or 2 moles of chymotrypsin, stoichiometrically.
|
P01065
|
Q5ZJN1
|
RTF2_CHICK
|
Replication termination factor 2 domain-containing protein 1
|
Gallus
|
MGCDGGTIPKRHELVKGPRKAVKVDKTAELVARWYYCTLSQEKLCRPIVACELGRLYNKDAVIEFLLDKSADKTPMEAASHIKSLKNVTELNLADNPAWSGDKESKKGDTYDDIQSARFICPVVGLEMNGRHRFCFLRNCGCVFSERALKEIKTEVCHKCGVPFQEEDVIILNGNKEDVEVLKKRMEDRRLKSKLEKKSKKCKSAESAAQQVTTEDSPGPSKVKNSKDCIASSSGEKRHIIFTKSSDDRSSSVPGKVNKASTATKRSIADTATRNLRHTNLFTTHSSAKRPKEECSNWVTHTAYCF
|
Replication termination factor which is a component of the elongating replisome. Interacts with nascent DNA.
|
Q5ZJN1
|
Q57920
|
HJC_METJA
|
Holliday junction resolvase Hjc
|
Methanocaldococcus
|
MRHKYRKGSSFERELKRLLEKEGFAVIRSAGSKGVDLIAGRKGEVLIFECKTSSKTKFYINKEDIEKLISFSEIFGGKPYLAIKFNGEMLFINPFLLSTNGKNYVIDERIKAIAIDFYEVIGRGKQLKIDDLI
|
A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.
|
Q57920
|
P20229
|
VKTTI_NAJNA
|
Venom trypsin inhibitor
|
Naja
|
RPGFCELPAAKGLCKAHKPAFYYNKDSHRCQKFIYGGCGGNANRFRTIDECNRTCVG
|
Serine protease inhibitor that inhibits trypsin (Ki=0.0035 nM).
|
P20229
|
A1UU01
|
MUTL_BARBK
|
DNA mismatch repair protein MutL
|
Bartonella
|
MIIRHLSENIINQIAAGEVIERPANVIKELVENAIDAQATRIEISIVNGGKNFIRVSDNGCGIPADQLTLAVSRHCTSKIVDDVSNICFLGFRGEALPSIGSVAKLKLTSRTQDADNANEISVIAGKIEGPKPAAANPGTIVEVRDLFFVTPARLKFMKTDRAETSAITDMIKRIAIAFPHIRFSLSSTDRMLMEFPATENNTQGQLQRITQIMGKEFAPNSIALNAERESVRLTGFTCLPSFNRSNSLHQFAYVNGRPVRDKLLWGAIRGAYADAIARDRHAVSIIFIDLPPADVDVNVHPTKADVRFRDPGLIRGLIIGAIHEALHQAGVRHTSTHSESVLTAFQIHPLENLKSAQRPFSYTSQPYHRVSTTTSMLQKPLDDSIDLREGIVPMMECLSAPSSDTRATIQTSPTEELHYPLGAAKAQIHKNYIISQTQDSLIIVDQHAAHERLVYEALKNALYSKPLSSQLLLIPEIVELSEEDAACLLTHKDSLQKFGLGIEPFGPGAILVRETPAMLGEINAQALIKDLADEAAEYDTTNNLKAMLDYVAATMACHSSVRSGRLLRPEEMNALLRQIEETPHSSTCNHGRPTYIELKLADIERLFGRK
|
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
|
A1UU01
|
Q03IF5
|
RS19_STRTD
|
30S ribosomal protein S19
|
Streptococcus
|
MGRSLKKGPFVDGHLMKKVEAQANDEKKKVIKTWSRRSTIFPSFIGYTIAVYDGRKHVPVYIQEDMVGHKLGEFAPTRTYKGHAADDKKTRR
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q03IF5
|
A3MA23
|
PSD_ACIBT
|
Phosphatidylserine decarboxylase beta chain
|
Acinetobacter calcoaceticus/baumannii complex
|
MSFTSRLKKELFIKAQNLVPQHQLSRVVGKVAASENPILKAAVIHAFKTKYGIDLSIAEQGNALKYKSFNDFFTRALKDGVRLVDENPDSIVSPADGAISQIGKITAGEVFQAKGQSFSVEKLIGDPQLAQPFQEGEFATVYLSPRDYHRVHMPFSGTLTETLYVPGELFSVNQVTAENVPGLFARNERMVCLFDTELGRMAVVLVGAMIVAGIETVATGKVKPSGRIELQHHELKLEKGAELGRFYLGSTAIILFEKDKIEWEKRYKAESVVVMGERMGHTL
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
|
A3MA23
|
Q8G4L8
|
ISPH_BIFLO
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
|
Bifidobacterium
|
MTADSCNPCLTLENTIDVQEVPMTKSVVLADPRGFCAGVDRAILTVQTILKAAEASGKRTREDGLPPVYVRRQIVHNKHVVEDLAGQGAVFVQELAEIPDAAAQAGIPVVFSAHGVSPVVKAEAERRGMHVVDATCPLVGKVHREVLRFVREGYEIVYIGHKGHDEAVGVVGESPEHVHLIEHESDVDSLDFAPDTKLVLLSQTTLSVDETADTIAALKAKFPWIQEPPSSDICYATSNRQAAVKLVAQQSDCVVIVGSANSSNSVRLMEVAQEGLGERGKAYRVDDASELDPAWFEGLESVGISSGASVPDELVSGVIDALQNLGFTGMKSVETIKENMHFVLPAELRRKK
|
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
|
Q8G4L8
|
A0AIR6
|
YBEY_LISW6
|
Endoribonuclease YbeY
|
Listeria
|
MPVLEIDLLDETNKLLDEDKQLVENILQFAAGYLKIDEGTELSLTFTTNEGIREINREYRNKDQATDVISFALEEMGEGETEIDWADFDLETPKMLGDIIISTEKAEEQAKDYGHTKARELGFLAVHGLLHLLGYDHMEPDEEKIMFGLQKEVLDAYGLER
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
A0AIR6
|
O75363
|
BCAS1_HUMAN
|
Novel amplified in breast cancer 1
|
Homo
|
MGNQMSVPQRVEDQENEPEAETYQDNASALNGVPVVVSTHTVQHLEEVDLGISVKTDNVATSSPETTEISAVADANGKNLGKEAKPEAPAAKSRFFLMLSRPVPGRTGDQAADSSLGSVKLDVSSNKAPANKDPSESWTLPVAAGPGQDTDKTPGHAPAQDKVLSAARDPTLLPPETGGAGGEAPSKPKDSSFFDKFFKLDKGQEKVPGDSQQEAKRAEHQDKVDEVPGLSGQSDDVPAGKDIVDGKEKEGQELGTADCSVPGDPEGLETAKDDSQAAAIAENNNSIMSFFKTLVSPNKAETKKDPEDTGAEKSPTTSADLKSDKANFTSQETQGAGKNSKGCNPSGHTQSVTTPEPAKEGTKEKSGPTSLPLGKLFWKKSVKEDSVPTGAEENVVCESPVEIIKSKEVESALQTVDLNEGDAAPEPTEAKLKREESKPRTSLMAFLRQMSVKGDGGITHSEEINGKDSSCQTSDSTEKTITPPEPEPTGAPQKGKEGSSKDKKSAAEMNKQKSNKQEAKEPAQCTEQATVDTNSLQNGDKLQKRPEKRQQSLGGFFKGLGPKRMLDAQVQTDPVSIGPVGKSK
|
Required for myelination.
|
O75363
|
O74435
|
CDC31_SCHPO
|
Cell division control protein 31
|
Schizosaccharomyces
|
MFANARAKRRSRASSPTPARLGGYAPLRVEITEEQRQDINEAFKLFDSDKDNAIDYHELRAAMRALGFNAEKSEVLKILRDFDKTGKGYLQMEDFVRVMTEKIVERDPLEEIKRAFELFDDDETGKISLRNLRRVAKELNENIDDQELEAMIEEFDLDQDGEINEQEFIAIMMDEA
|
Required for the proper coordination between exit from mitosis and the initiation of septation. Has a role in bipolar spindle formation during spindle pole body (SPB) duplication. Required for the localization of sad1 to the SPB .
|
O74435
|
P00606
|
PA2A_BUNMU
|
Phosphatidylcholine 2-acylhydrolase
|
Bungarus
|
MNPAHLLILSAVCVSLLGAANVPPQHLNLYQFKNMIVCAGTRPWIGYVNYGCYCGAGGSGTPVDELDRCCYVHDNCYGEAEKIPGCNPKTKTYSYTCTKPNLTCTDAAGTCARIVCDCDRTAAICFAAAPYNINNFMISSSTHCQ
|
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
P00606
|
P98052
|
COX2_THETH
|
Cytochrome cba3 subunit 2
|
Thermus
|
AYTLATHTAGVIPAGKLERVDPTTVRQEGPWADPAQAVVQTGPNQYTVYVLAFAFGYQPNPIEVPQGAEIVFKITSPDVIHGFHVEGTNINVEVLPGEVSTVRYTFKRPGEYRIICNQYCGLGHQNMFGTIVVKE
|
Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
|
P98052
|
B1X0W5
|
PLSY_CROS5
|
Lysophosphatidic acid synthase
|
Crocosphaera subtropica
|
MAFLISALLILIGYLLGSIPTGYLTGLHLKGIDVRQHGSGSTGATNILRTIGKRAAIFVLTVDLAKAMLAVILVKLWFFVESPEMIPLEWKSWLVVFAAIAAVLGHSKSIFLNFTGGKSVASSLGVLLVLNPIVALGTLGSFLAMLSLSRIVSLSSITGVVAVNVLMFGLHQPLPYCLFGVIVGLYVTFRHRTNIIRLLQGTEPRLGQKLQQEGS
|
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
|
B1X0W5
|
P14668
|
ANXA5_RAT
|
Vascular anticoagulant-alpha
|
Rattus
|
MALRGTVTDFSGFDGRADAEVLRKAMKGLGTDEDSILNLLTARSNAQRQQIAEEFKTLFGRDLVNDMKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTDEKVLTEIIASRTPEELRAIKQAYEEEYGSNLEDDVVGDTSGYYQRMLVVLLQANRDPDTAIDDAQVELDAQALFQAGELKWGTDEEKFITILGTRSVSHLRRVFDKYMTISGFQIEETIDRETSGNLENLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVIVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGGEDD
|
This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.
|
P14668
|
Q1LPX5
|
PSD_CUPMC
|
Phosphatidylserine decarboxylase beta chain
|
Cupriavidus
|
MNYPHPLIAREGWPFLAGAFIVSVLVHISAGFWGALPLWIVTLFVLQFFRDPPRPIPSAPNAILAPADGRIVVVEKTQDPYAGREALKISVFMNVFNVHSNRSSLDGKVEKLEYFPGKFVNADLDKASMENERNAVVIRRASDGQVVTLVQVAGLVARRILCYINVGDMLSRGQRYGFIRFGSRVDVYLPTDARPRVTIGEKVSASATVLADLDVRA
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
|
Q1LPX5
|
Q7JUY7
|
CED6_DROME
|
Cell death protein 6 homolog
|
Sophophora
|
MPYQPANSGGTSGGSKAAAKMAQLKFWNKQNSSKQQQQDKDKDAADGGNNTSGGGTGSNSNGDAKSEAKNGKRNWLHTPEQLISGHAVYLVKFFGNLSVDQPKGIEVVKEAIRKLQFAQQMKKAETGTQEKFKKLEITISIKGVAIQEPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKTVKTQDGSDPTSNGHANGNGDGSAKVEESHECFVFISNKLASDITLTIGQAFDLAYRKYMDSTEKTNLSKAQQQINHLQQTVNVYKERLREVSAKLPKAELDALLFNLGIKDILEAPTTEPQNGIEVASEALSNGKLDDDKLLIDTNSTTASTHSASPSSFLPIVPPRNNLSSQISIGGKSNSQKMDELLLNSDSDSDFDPRADETQEIGGTGRSAISNMFGFEPANSFGQHLFSNNNDHKLQNNNSSLLITSNNNSINSSGFSSELNITPPLLAPPPKIAAPRRLNSVTTGNGLNGNTDLFGSDPFELNNGPNIFKQNQLNLDDFSLESLDPLRK
|
Plays a role in axon pruning in larval mushroom body neurons during metamorphosis . Plays a role in the infiltration of glial cell processes into mushroom body lobes and the subsequent engulfment of degenerating axon branches . Involved in Drpr-mediated phagocytosis of apoptotic cells . Required for bacterial phagocytosis . During neuromuscular junction development, required for the clearance of pruned ghost boutons and presynaptic debris and for normal synaptic growth .
|
Q7JUY7
|
A0RPZ6
|
QUEA_CAMFF
|
Queuosine biosynthesis protein QueA
|
Campylobacter
|
MSDIFSLSSYDYKLPQDLIATAPTMPKEEARLLVYDRQKDSVFHLKFKNLSEILPECAIIFNDTKVIKARIYGRKDSGAEIQMLLNQPLQNSLFSCYIRGKVKVGTKLKFDLGVEAEVLELKDDSSRIVKFKKNEQILNTSEIYNILSHIGHVPLPPYIKREDTPDDEIWYQSIFAKNEGAVAAPTASLHFNDQMLDDLNKTHDISYITLHVGAGTFKGVEHCDIREHKMHSEFYCISKKAKNIIDSDIKLLGVGTTVTRCIEYYYRTKQPKGFCDLFLHPDNKPLRQDFLLTNFHLPKSTLIMLVASFIGLEKTMEIYKQAVENRYKFYSYGDGMLII
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
A0RPZ6
|
P61188
|
HTPG_TREDE
|
High temperature protein G
|
Treponema
|
MAQYKFETEVNQLLSLIIHSLYSNKEIFLRELVSNASDALDKLKYLTLSDEAYKQIKFEPRIDICFDDTANTLTVRDTGLGMNEEDLKNNLGTIARSGTKAFLDQLAAADKKDSNLIGQFGVGFYSAFMAASTIDVISKKAGENDVWKWTSDGKGAYDLEKVDDTAFPIIDGVPEGANGTCVILHLNNEDSEYATRWRIEEIIKTYSDHIAFPIYLHFTEKQYDDKGKVKSEASKTEQINDAGAIWQKPKSELKEEDYFNFYKSLSHDSQEPLLYVHTKAEGTQEYTTLFYVPSKAPFDMFHADYRPGVKLFVKRVFITDDEKELLPTYLRFVRGVIDSEDLPLNVSREILQQNRILSNIKNASVKKLLGEFKKLAENDKEKYNKFIAEFNRPLKEGLYSDYEHREELADLVRFKTTSPEVKEDEWTSFADYVSRMKSDQKAIYYITGEDEKTLRQSPHLEVYKQKGFEVLIMPDEIDDIIIPSLGKYKDWELKAANRAGSDKELNTEEETKEAEKKEKDFKPVLEKIKEVLGDKVKEVRFSKRLSDSPSCIVVDETDPSLQMERMMRAMGQFNTSAVKPILEVNADHPLVQKLKDSKDKEFVEDMSNLLLEQALLVESGELKAPVDFVKRLNRLMTNLK
|
Molecular chaperone. Has ATPase activity.
|
P61188
|
Q1GH67
|
KGUA_RUEST
|
GMP kinase
|
unclassified Ruegeria
|
MAHSKAQRRGLLIILSSPSGAGKSTLAKRLRAWDSDISFSVSATTRKPRPGEVDGQDYHFVTVESFKQDVANGDMLEHAHVFGNFYGSPKGPVQTAINEGRDVLFDIDWQGAQQITNSDLGKHTLSIFLLPPSITELRRRLESRGQDDAETISRRMQKSWDEISHWGSYDHVLINEDLDETEEALKTIITATRLRRIQQPSLIEHARALQQEFEDLS
|
Essential for recycling GMP and indirectly, cGMP.
|
Q1GH67
|
Q7S232
|
MCA1A_NEUCR
|
Metacaspase-1A
|
Neurospora
|
MSYGYPGQGYGPGGGHHQPPPPQWDGQQQHHHQGGYGYSNPGQGQYNPQPPQDQGYGGYHQQPPQQYQQGSYNQGQYPPQGGYGGPYGQQQQHHQQGHSQRPPGPPPDGYDIYGYPIGSGHQTRNQGSHEIHEIPSGTQQFGHGAPEGYGFQYSNCSGRRKALLIGINYLGQDAELHGCINDTKNVSAFLVENYGYKREDMVILTDDATNPLLQPTKENILRAMQWLVAGAQPNDALFLHYSGHGGQTKDTDGDEDDGYDEVIYPVDFKTAGHIVDDQIHDTVVKPLQPGVRLTAIFDSCHSGSVLDLPYIYSTKGVIKEPNLAKEAGQGLLAAVGSYARGDIGGMASSLFSVAKTAFGGGNEAYERTKRTKTSPADVIMWSGSKDDQTSADATIASQATGAMSWAFITAIKANPKQSYVQLLNSIRDVLETKYTQKPQLSSSHPIDVDMLFVM
|
Involved in cell death (apoptosis).
|
Q7S232
|
O83387
|
RL25_TREPA
|
General stress protein CTC
|
Treponema
|
MDERRLKGKRRVQLGKYAAVRGRKEGRLPAVMYDHRGVSVPLELAQQDFDRLFRALTRSTVLSLELDGGEVFCVFVKDYQHNMVSDRVEHVDFYAVEESVPLRMRIRLQLCGSPEGVRYGARLEKGLSYIEVESLPRNLPDRVVLDISGLGAGDVRRVRDVPLPASVVVLSDPDAVIVALSSSASEAGSPAGARTG
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
O83387
|
Q23982
|
PEB2_DROME
|
PEB-meII
|
Sophophora
|
MIRILVLMITFTLMTGSALCSIEQLMRVFGGGSVGGGSRLDINRRVTIVPPEGELSFGYGFRPGFY
|
Protein component of the posterior mating plug.
|
Q23982
|
P66412
|
RS14Z_STAAN
|
30S ribosomal protein S14 type Z
|
Staphylococcus
|
MAKTSMVAKQQKKQKYAVREYTRCERCGRPHSVYRKFKLCRICFRELAYKGQIPGVRKASW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
P66412
|
Q45585
|
SIGW_BACSU
|
RNA polymerase sigma-W factor
|
Bacillus
|
MEMMIKKRIKQVKKGDQDAFADIVDIYKDKIYQLCYRMLGNVHEAEDIAQEAFIRAYVNIDSFDINRKFSTWLYRIATNLTIDRIRKKKPDYYLDAEVAGTEGLTMYSQIVADGVLPEDAVVSLELSNTIQQKILKLPDKYRTVIVLKYIDELSLIEIGEILNIPVGTVKTRIHRGREALRKQLRDL
|
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Sigma-W controls genes involved in response to cell envelope stress such as antimicrobial peptides , alkaline pH , transport processes and detoxification.
|
Q45585
|
Q6NKZ8
|
C14A2_ARATH
|
EUI-like P450 A2
|
Arabidopsis
|
MESLVVHTVNAIWCIVIVGIFSVGYHVYGRAVVEQWRMRRSLKLQGVKGPPPSIFNGNVSEMQRIQSEAKHCSGDNIISHDYSSSLFPHFDHWRKQYGRIYTYSTGLKQHLYINHPEMVKELSQTNTLNLGRITHITKRLNPILGNGIITSNGPHWAHQRRIIAYEFTHDKIKGMVGLMVESAMPMLNKWEEMVKRGGEMGCDIRVDEDLKDVSADVIAKACFGSSFSKGKAIFSMIRDLLTAITKRSVLFRFNGFTDMVFGSKKHGDVDIDALEMELESSIWETVKEREIECKDTHKKDLMQLILEGAMRSCDGNLWDKSAYRRFVVDNCKSIYFAGHDSTAVSVSWCLMLLALNPSWQVKIRDEILSSCKNGIPDAESIPNLKTVTMVIQETMRLYPPAPIVGREASKDIRLGDLVVPKGVCIWTLIPALHRDPEIWGPDANDFKPERFSEGISKACKYPQSYIPFGLGPRTCVGKNFGMMEVKVLVSLIVSKFSFTLSPTYQHSPSHKLLVEPQHGVVIRVV
|
Involved in the inactivation of early gibberellin (GA) intermediates.
|
Q6NKZ8
|
Q8IX18
|
DHX40_HUMAN
|
Protein PAD
|
Homo
|
MSRFPAVAGRAPRRQEEGERSRDLQEERLSAVCIADREEKGCTSQEGGTTPTFPIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSPNRKEHLKVVVMSATMELAKLSAFFGNCPIFDIPGRLYPVREKFCNLIGPRDRENTAYIQAIVKVTMDIHLNEMAGDILVFLTGQFEIEKSCELLFQMAESVDYDYDVQDTTLDGLLILPCYGSMTTDQQRRIFLPPPPGIRKCVISTNISATSLTIDGIRYVVDGGFVKQLNHNPRLGLDILEVVPISKSEALQRSGRAGRTSSGKCFRIYSKDFWNQCMPDHVIPEIKRTSLTSVVLTLKCLAIHDVIRFPYLDPPNERLILEALKQLYQCDAIDRSGHVTRLGLSMVEFPLPPHLTCAVIKAASLDCEDLLLPIAAMLSVENVFIRPVDPEYQKEAEQRHRELAAKAGGFNDFATLAVIFEQCKSSGAPASWCQKHWIHWRCLFSAFRVEAQLRELIRKLKQQSDFPKETFEGPKHEVLRRCLCAGYFKNVARRSVGRTFCTMDGRGSPVHIHPSSALHEQETKLEWIIFHEVLVTTKVYARIVCPIRYEWVRDLLPKLHEFNAHDLSSVARREVREDARRRWTNKENVKQLKDGISKDVLKKMQRRNDDKSISDARARFLERKQQRTQDHSDTRKETG
|
Probable ATP-dependent RNA helicase.
|
Q8IX18
|
A7NBS2
|
HFQ_FRATF
|
RNA-binding protein Hfq
|
Francisella
|
MSRISSLQDPFLNALRKEKVSVSVYLVNGIKLQGQVEAFDQFCIVLRNTVNQMVYKHAISTIVPAKSVRMVYSSFNPYHQNSNDEQDENVDDIHSDDLEIQENEGNIHE
|
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
|
A7NBS2
|
Q8TYZ5
|
TMCA_METKA
|
tRNA(Met) cytidine acetyltransferase TmcA
|
Methanopyrus
|
MPDKAEVFFDEGVLDFADVDEIVLDVGEEALAEALAHRHRRMIVFQGDEGKAEAAGVVTAGAADVLFDVRDRPISVLYVTDSLKEDTYARERYEEFRRVLEGFAEEANFEYELEALTFSGSKRALGTTWDLMVIDLSYDLDPDAIGRLVETVRGGGLVIFQTPPFDRWRNMWTAFHKSLVTPPYTLDHVGKRFNRRFIRKLKEHDGVWIVDTDEWTAEPEPSEDVDLEVEVKRRERPDLDPPDDAVLPEELYRMCATEDQFRALIRFEELLESNGKTALILTADRGRGKSALLGIAVAGAGVTTDVYDVVVTASEPENVAVLFEFLLEALRELGVEYDVERDDKGNIVYVETDDFVVEYERPSEASEIECDLMVVDEAASIHVPILERILDNNDKVVYSSTIHGYEGAGRGFSVRFLQNVRKRRDVRLIEFKMHEPIRYDSDDPIERWLFDTLLLDAEPADLDKEDLECVKEMRVEFEKPDLRYWFEDPEGEEELRQFIGIYVMAHYRNRPSDVMVLADAPHHEAYALKTETGKIVTALQVAREGTIPRDVITKMRRGYRPPGNVIPDLMVQHHDALDFPRMKGLRIVRIATHPDIMRHGLGSRALKELAKIAKKKDYDWIGTGFGANEELTRFWLRNGFVPVHISPNRNPVSGEYSVAVIRPISEEAEEIINRANFEFRIKLADWLGETHRDLEPEVARLLFEPMSSLRYRPTLTEGQLRRLKKYADMVHTYEIAADAVRELAKAYFLDTEDRPELSEEEELLLITKCLQRWKWADVADVLGEEVPDLMRSLRDLVGLLYEEYKEDLQRSAAVEGIRKAVERLADKGLTGTVIVEVEEGEPKEVIIRREERLEL
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
|
Q8TYZ5
|
Q5SIP7
|
RRAAH_THET8
|
Regulator of ribonuclease activity homolog
|
Thermus
|
MEARTTDLSDLYPEGEALPMVFKSFGGRARFAGRVRTLRVFEDNALVRKVLEEEGAGQVLFVDGGGSLRTALLGGNLARLAWEKGWAGVVVHGAVRDTEELREVPIGLLALAATPKKSAKEGKGEVDVPLKVLGVEVLPGSFLLADEDGLLLLPEPPSGVRSGG
|
Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
|
Q5SIP7
|
Q3ALY0
|
UCRI_SYNSC
|
Rieske iron-sulfur protein
|
unclassified Synechococcus
|
MTQLSSSDVPGMGRRQFMNLLTFGSVTGVALGALYPVANYFIPPKAAGSGGGTSAKDELGNPITASGWLSSHPEGDRSLVQGLKGDPTYLIVEGEDAIGSYGINAICTHLGCVVPWNSGANKFMCPCHGSQYDSTGKVVRGPAPLSLALANVSVENDNVFVSQWTETDFRTGDKPWWA
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
Q3ALY0
|
P57130
|
RNPA_BUCAI
|
Protein C5
|
Buchnera
|
MLNYFFKKQLRLSDSTSFQDVFNGSVKKKNTLEISILGRFNLLGHPRLGLSIPRKNIKHAHNRNLIKRLVRETFRLLQYKLLSMDFVVIAKKNILFLNNTRIIDMLNSLWSNYYR
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
P57130
|
C1FW06
|
ORTA_UNKP
|
AKP thiolase
|
environmental samples
|
MSEKCKKDDWVEIHYVVLEARERTGDIPEDTRKVPLECWIKGWAEKEGTVGEEVTIRTPANRYVKGTLTRINPEYTHTFGPCASELSAIGQELRATLKEGK
|
Involved in the ornithine fermentation pathway. Catalyzes the thiolytic cleavage of 2-amino-4-ketopentanoate (AKP) with coenzyme A (CoA) to form acetyl-CoA and alanine. It is strictly specific for AKP.
|
C1FW06
|
Q9RVD6
|
SYW2_DEIRA
|
Tryptophanyl-tRNA synthetase II
|
Deinococcus
|
MPFVDLEVPTMTTPTPAATPARPRVLTGDRPTGALHLGHLAGSLQNRVRLQDEAELFVLLADVQALTDHFDRPEQVRENVLAVALDYLAAGLDPQKTTCVVQSAVPELAELTVYFLNLVTVSHLRQNPTVKAEIAQKGYGERVPAGFFVYPVSQAADIAAFGATLVPVGDDQLPMLEQTREIVRRFNALYAPVLAEPQAQLSRVPRLPGLDGQAKMSKSLGNAIALGDSADEVARKVMGMYTDPGHLRASDPGRVEGNPVFTFLDAFDPDPARVQALKDQYRAGGLGDVKVKKHLIDVLNGVLAPIRTRRAEYERDPDAVLRFVTEGTARGREVAAQTLGQVRRAMRLFGH
|
Catalyzes the formation of 5'adenyl-Trp and tRNA(Trp) but with 5-fold less activity than TrpRS. Increases the solubility of the nitric oxide synthase oxygenase (nos), as well as its affinity for substrate L-arginine and its nitric-oxide synthase activity. The complex between trpS2 and nos catalyzes the regioselective nitration of tryptophan at the 4-position.
|
Q9RVD6
|
Q7VKW2
|
UBIG_HAEDU
|
3-demethylubiquinone 3-O-methyltransferase
|
Haemophilus
|
MHNVDQQELSKFEQMAHSWWDPNGSFKPIHLLNPLRFNYIQTKANGLFGKKVLDVGCGGGILSEAMAQAGAIVTGIDMTTEPLEIAKQHAIENGLTIHYQQTTVEDLRLNHTACNAEKFDVVTCMEMLEHVPDPLSVIQSCKALLKPDGVLFLSTINRTLKAYMLVVIGAEYLLKMLPKGTHEFEKFIKPAELLTWCDQASLECKEMKGYHFNPLTEKFWLNNDVSCNYIAMLKAK
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
Q7VKW2
|
B6IZ80
|
GLYA_COXB2
|
Serine hydroxymethyltransferase
|
Coxiella
|
MYEPTLTVESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYAGCEFVDIAEQLAIDRAKELFGADYANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPVSFSGKFYKAVHYGLNAHGDIDYEQAAQLAQEHKPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLILAKANPELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERDYTIVSGGTQNHLFLVSLLNKNISGKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWVCDILDDIHNEKVIADVKQKAHELCGKFPVYQELD
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
B6IZ80
|
C0R2W3
|
CLPP_WOLWR
|
Endopeptidase Clp
|
unclassified Wolbachia
|
MTLIPIVVEQTSRGERAYDIYSRLVKERIIFVTGPIEDNMASVIVAQLLFLESENPDKDICMYINSPGGVVTAGLSIYDTMQYINPDVSTLCIGQAASMGSLLLAAGTKGKRYSLPHSRIMIHQPSGGYHGQATDIEIHANEILRVKKKLNQIYEKHTGNSLKKIEGMMERDKFMDPEEARKIGLIDRVIAERTDIEIENIKVKQKVG
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
C0R2W3
|
Q4QJU5
|
PDXS_HAEI8
|
Pdx1
|
Haemophilus
|
MAENRYELNKNLAQMLKGGVIMDVQNPEQARIAEAAGAAAVMALERIPADIRAVGGVSRMSDPKMIKEIQGAVSIPVMAKVRIGHFVEAQILEAIEIDYIDESEVLSPADNRFHVDKKEFQVPFVCGAKDLGEALRRIAEGASMIRTKGEPGTGDIVQAVRHMRMMSQEIRRIQNLREDELYVAAKDLQVPVELVQYVHKHGKLPVVNFAAGGIATPADAALMMQLGAEGVFVGSGIFKSGDPIKRASAIVKAVTNYRNPQILAQISEDLGEAMVGINENEIQILMAERGK
|
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
|
Q4QJU5
|
A9VQ67
|
WHIA_BACMK
|
Probable cell division protein WhiA
|
Bacillus cereus group
|
MSFASETKKELTNLEMKECCEKSELSALLRMNGSLSFSNRRLSIDIQTENAAIARRIYTLLKKGYDVTVELLVRKKMRLKKNNVYIVRLVEKSREILADLHIVRDDFSFIRNISQELIEKKCCKRSYLRGAFLAGGSVNNPETSSYHLEIFSLYKEHNDSICELMNGFDLNSKTLERRKGYITYLKEAEKITEFLNIIGAHNALLRFEDIRIVRDMRNSVNRLVNCETANLNKTIGAALRQIENIRYIDETVGLDILPDKLREIAQLRRDYQDVTLKELGEMVSGGKISKSGINHRLRKIDEIAEKLRAGETVAKK
|
Involved in cell division and chromosome segregation.
|
A9VQ67
|
Q0TSZ6
|
AZOR_CLOP1
|
FMN-dependent NADH-azoreductase
|
Clostridium
|
MSKVLYIKANIKNEGESRTFKVSDSFVEEYKKNNPEDEIITLDLYKENIDFLRADDLGKLFGPKDEESKNNSILKYAYQFADADKYIIAAPMWNLSFPAILKAYIDYVSVSGITFKYTAEGPVGLLNNKKAVHIVSRGGGYDNSPYEMGDRYLRTILGFFGIKDIETIAIDNLDVMGVNVEEKVEEGIEKAISLAKKF
|
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
|
Q0TSZ6
|
A7ZCH3
|
FOLD_CAMC1
|
Methenyltetrahydrofolate cyclohydrolase
|
Campylobacter
|
MKILDGKAVSLKVKESVKVRADELKKFGVEPTLAVVLVGEDKASQTYVRAKEKACNEYGIKSVAHRLSENTTQNELLALINVLNLDDSIHGILVQLPLPKHIDTNVVLAAIDPRKDVDGFHAVNVGKLVSGLDGFVPCTPLGVMEILKEYGIEVAGLNAVVIGRSNIVGKPMANLLLNASATVTVTHSKTKNLKEICKNADLIVAAIGKPFFLKADMVKDGAVVVDVGINRLDDGRLVGDVDFDEVAPKCSYITPVPGGVGPMTIAMLLNNTILAAQAKIAKN
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
A7ZCH3
|
Q8W4D8
|
DDL_ARATH
|
Protein DAWDLE
|
Arabidopsis
|
MAPSSRSPSPRTKRLRRARGEKEIGRSREREDDGREREKRNSRERDRDIGRDRDRERKGEGERDREVGDKRRRSGREDTEKRRRTRTDDERYSRGRHERSTSPSDRSHRSSRRSPERAIASRHDEGSNARGGSEEPNVEEDSVARMRAVEEALAAKKKEEPSFELSGKLAEETNRYRGITLLFNEPPEARKPSERWRLYVFKDGEPLNEPLCLHRQSCYLFGRERRIADIPTDHPSCSKQHAVIQYREMEKEKPDGMMGKQVKPYIMDLGSTNKTYINESPIEPQRYYELFEKDTIKFGNSSREYVLLHENSAE
|
Involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. May facilitate DCL1 to access or recognize primary miRNAs. Binds RNA non-specifically.
|
Q8W4D8
|
Q083F6
|
KDSB_SHEFN
|
CMP-8-amino-3,8-dideoxy-manno-octulosonate synthase
|
Shewanella
|
MKVTLLIPARYGSSRFPGKPLAPINGKPMIQHVYERASLAKGLDSIYVATDDDRIKDAVESFGGKVVMTSPDAASGTDRINDAIALLGLNDDDLVINLQGDQPLIDPISIEQIISLFERHPGEFEMATLGFEIVDKRELDDPMHVKMVFDNDHNALYFSRSRIPFGRDTNDYPVYKHLGVYAYTKRFVNAFAKLPLGRLEDLEKLEQLRALEYGHKIKIAISAFDSPEVDTPEDIRKCELRLAVD
|
Activates KDO8N (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in the Shewanella genus.
|
Q083F6
|
A9MMA3
|
GLGA_SALAR
|
Starch [bacterial glycogen] synthase
|
Salmonella
|
MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGIDVRVLLPGFPDIRRGIPDAHVVSRRDTFAGKISLLFGHYNGVGVYLIDAPHLYERPGSPYHDTNLYAYTDNVLRFALLGWVGCEMACGLDPFWRPDVVHAHDWHAGLAPAYLAARGRPAKSVFTVHNLAYQGMFYAKHIDDIELPWSFFNMHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLLRQRHLEGRLSGVLNGVDEKIWSPESDLLLASRYTRDTLEEKAENKRQLQIAMGLKVNDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEHPGQVGVQIGYHEAFSHRIMGGADIILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVSDSSLENLADGIASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMAMDFSWQVAAKSYRELYYRLK
|
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
|
A9MMA3
|
Q7VF74
|
DNLJ_HELHP
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Helicobacter
|
MTSQEYYTQVQILKKMAYHYYVLDEPIATDEQYDSLYHQIVRFEEENPHLIDASSPTQRVGDVPLESFSKNTHLERMWSLEDVFNYDELVEWVQRIYKSYPQATFTCSPKFDGASLNLLYQEGKLVSATTRGDGVIGELVTHNAKTIQSIPLEINYKEEIEIRGEVVIAKEDFEYINQDRLSENLSLFANPRNAAAGSLRQLDAKITAKRKLRFMPWGIGAGLIRFESFYEAFNTITRLGFAPVPFLSYCESIESIQNAYNVLFSQRNNYPIMLDGMVIMLDKIASQQQLGWTIKSPRFACAYKFPAVEKSSKILSVSLQVGRTGIITPVAELKPVEIEGAMISRATLHNFSEIERKDIRLGDEVIIIRSGDVIPKIIKPLVALRDGTQKVISKPTHCPVCGEELLLEDIFIKCQNLSCEARVIESIIHFASKKALNIDGLGEKIVIQLYENAFVRNIKDIYALSIQQLLTLEGWQEKRANNLIYAIQNTIGVELWRFINALGIEHIGEGASKKLAQKFGLNVFELELSEILSVDGFGEEMAYSLVEFNHANKTLIAELLCIIKPKVELLEIDNNNVFFNKTIVLTGTLSQPRDRIIKLLESKGAKISSSVSKKTDFVIYGEKAGSKLEKAQSLNITTLNEEEFLAQINK
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
Q7VF74
|
Q65T42
|
CYSA_MANSM
|
Sulfate-transporting ATPase
|
Basfia
|
MSIKIENLEKHFGSFHALKNINLQFKQNQLTALLGPSGCGKTTLLRIIAGLEFADSGKILFEHRDVTDLSAKDRGVGFVFQHYALFQNMTVYDNVAFGLRVKPRKERPSKEEIQQKVTALLKLVKLDWLANAYPNQLSGGQRQRIALARSLAVQPKVLLLDEPFGALDAQVRKELRRWLRDLHQELNVTSIFVTHDQDEALDVSDRIVVMNQGQIEQIDEPNQIYHAPQTPFVTQFVGDVNVFHGHIDEGNLVIGEFSHKIDPATNTTQPVNNQSATAYIRPYELTISRHADNALATGKITHINAIGFIVRIEIESAQSDQPIEVILTKAAYSQSQYKVNEQIYLVPDKLNLFQQMNI
|
Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
|
Q65T42
|
Q1GK29
|
RL22_RUEST
|
50S ribosomal protein L22
|
unclassified Ruegeria
|
MGKDKNPRRVADNEAMAKVRMLRTSPQKLNLVAQMIRGKKVDKALTDLTFSNKRIAQDVKKCLQSAIANAENNHNLDVDELIVAEAWVGKNLTMKRGRPRARGRFGKILKPFAEITIKVRQVEEQA
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
Q1GK29
|
Q10S44
|
BH003_ORYSJ
|
bHLH transcription factor 3
|
Oryza sativa
|
MELDEESFLDELMSLRRDGSAPWQAPPYPGGGGGGGGGGMMMSDLLFYGGDGGSAEARGGMDASPFQELASMAAPPPQHPHEEFNFDCLSEVCNPYRSCGAQLVPSEAASQTQTQLTPLRDAMVAEEETSGDKALLHGGGGSSSPTFMFGGGAGESSEMMAGIRGVGGGVHPRSKLHGTPSKNLMAERRRRKRLNDRLSMLRSIVPKISKMDRTSILGDTIDYVKELTERIKTLEEEIGVTPEELDLLNTMKDSSSGNNNEMLVRNSTKFDVENRGSGNTRIEICCPANPGVLLSTVSALEVLGLEIEQCVVSCFSDFGMQASCLQEDGKRQVVSTDEIKQTLFRSAGYGGRCL
|
Transcription factor involved in defense responses that functions downstream of RAC1 and upstream of PAL1 and WRKY19 genes.
|
Q10S44
|
Q6MGM7
|
ATPB_BDEBA
|
F-ATPase subunit beta
|
Bdellovibrio
|
MAFGKVKQVMGPVVDVEFEGGELPAINSALRVSNKFISDVEFNLVLEVAQHLGDGVVRTISMDQTEGLVRGEKVKALGTQITAPVGREALGRIINVVGEPIDEMGPVNAKEQWGIHRTAPKFEDQATAAAMLMTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELIRNIATEHGGFSVFAGVGERTREGNDLWQEMKQSGVLAKTSLVFGQMNEPPGARARVALTGLTVAEYFRDVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATEMGTLQERITSTKKGSITSVQAVYVPADDYTDPAPATTFTHLDATTNLDRDIAAMAIFPAVHPLTSTSRLLDPTVIGEEHYKCARDVQALLQRNRELQDIIAILGMDELSESDKLVVSRSRKIQRFLSQPFFVAEQFTGLPGKYVDIKDTVKGFREILDGKHDALPEQAFYLVGTIEDAIEKAKKLQA
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q6MGM7
|
Q54K66
|
PNO1_DICDI
|
RNA-binding protein pno1
|
Dictyostelium
|
MTEVIETKEVENIISEQSLKTESVKVSNKRSRDDEEMKDSEGGVKKTSFPQISVEDTEEEQIRKVTIPFNRIAPLKANWQQIYEPIVTHLKLQIRMNTKTRKVELKTSKSTKETSALQKAADFVHAFSLGFEVNDAVAILRLDDLYIDSFDVEDVKILKGDNLSRAIGRVAGKDGKTKFTIENVTKTRIVLADKRIHILGSYSNIRVAKDAICDLIIGSPPGKVYAKLRTVSSRIAERF
|
Positively regulates dimethylation of two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA.
|
Q54K66
|
Q5P201
|
CLPS_AROAE
|
ATP-dependent Clp protease adapter protein ClpS
|
Aromatoleum
|
MATQKQDEFLLETEQTRTKPPPLYKVLLLNDDFTPMDFVIVVLQKFFGMDRERATRVMLQVHREGMGVCGVFPKDVAATKVEQVVAFARQHQHPLACVMEEN
|
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
|
Q5P201
|
Q825U9
|
DEF3_STRAW
|
Polypeptide deformylase 3
|
Streptomyces
|
MASESDRTVPDTRSASRPLADRVEELLATGGPLPIVAAGDPVLRRGAEPYDGQLGPGLLARFVEALRLTMHAAPGVGLAAPQVGVGLRIAVIEDPAPVPEEVGAVRGRVPQPFRVLVNPSYEAVGSDRAAFFEGCLSVPGWQAVVARPARVRLTALDEHGRAVDEEFTGWPARIVQHETDHLDGMLYLDRAELRSLSSNEAMALRWSQPTPERAAAALGFALPD
|
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
|
Q825U9
|
Q5KQN0
|
CAX2_ORYSJ
|
OsCAX2
|
Oryza sativa
|
MMGAEKAEGMEELELEEGGGSPSPSPMTAAGKMQALDFEHIGSLAAVAESLSTGSKWRRALTSVRVVILQAKINVLLPFGPLAVMLHYLSANHQGWVFLFSLIGITPLAERLGYATEQLALYTGPTIGGLLNATFGNATEMIISLYALKNGMIRVVQQSLLGSILSNMLLVLGCAFFAGGLVHPSRDQVFNKASAVVNSGLLLMAVLGLMFPAVLHFTHSEVQYGKSEVSLSRFSSCIMLVAYASYLFFQLKSQRSLYSPIGEQEEEVTEDEEEEKEITQGEAICWLFVLTIWISILSGYLVDAIQGASESLNMPVAFISVILLPIVGNAAEHASAIMFAMKDKLDITLGVAIGSSTQISMFVIPFCVVIGWIMGQQMDLNFQLFETATLFITVLVVAFMLQEGTSNYFKGLMLILCYLIVAASFFVHVDPDSSNNK
|
Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase.
|
Q5KQN0
|
Q90YJ9
|
CLAT_CHICK
|
Choline O-acetyltransferase
|
Gallus
|
MPDLEKDMQKKEKDSRSKDEPAVPKLPVPPLQQTLQMYLQCMKHLVPEEQFRKTKSIVEQFGVAGGLGESLQLILEERREETTNWVFNYWLDDMYLNNRLALPVNSSPAIIFARQNFKDVNDQLRFAANLISGVQDYKALLDSHALPVDFARGQLSGQPLCMKQYYGLFSSYRLPGHTKDTLVAQKSCVMPEPEHIIVACNNQLFVLDVGINFRRLSEGDLFTQLRKIAKMAENEEEMLPPIGLLTTDGRTEWAEARTILMKDSTNRDSLDMIERCICLVCLDGTSGVELNDTNMALQLLHGGGYHKNGANRWYDKPMQFVVGRDGVCGTVCEHSPFDGIVLVQCTEHLLKHMKESSKKLLRADSVSELPAPRRLRWKCSPEIQAHLASSAEKLQRIVKNLDFIAYKFVNYGKEFIKKQKTSPDAYIQVALQLAFYRCHRRLVPTYESASIRRFDEGRVDNIRSATAEAFAFVKAMIDDKPALSDSEKMQRFKDAIAAQTNYTILAITGMAIDNHLLGLREVAREHFKELPEIFTDETYLTSNRFILSTSQVPTPMEMFCCYGPVVPNGYGACYNPQPEHILFCISSFKDCKETSSDMLAKAVEESLLEIRDLCNKCSSSTAKSLAKQEEATQLRSDRKL
|
Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
|
Q90YJ9
|
P29347
|
MTS1_STRSA
|
Type II methyltransferase M.StsI
|
Streptococcus
|
MRYIGSKKLLLPEIKKMVDKHTDGSEEVFLDLFAGTNVVANYFKQFYTVYSNDMLFFSYVNAKATIENNSKPSFSKLIQAGISSPMTYLQNLEVNDETIGYYEVAYSPTGEANYLSVHNAKKLDIIRSQIESWKNQNLLTEHEYYYLLSSLIEALPFISNTTGTYGAFLKHWDKRSLNDLELQDFTIFDNSKQNKAFNEDANELVQKIKADIVYIDTPYNSRQYASNYHLLENVARNEHPTLKGITKIFDWKNLKSDYATKGKALVAMRDLIQNINSTHIILSYNNEGIISEEDLTNILKEFSVDGIVDIKKIPYRKYQSKNVSKNKEIYELLFYIQRKPFSKNKTLNKPLNNVRVSSTKKYIKSPLNYIGGKYKLLNQILPLFPKNINTFVDIFSGGANVGINVKAKKYIFNDMNTRINEMFRYFQTQPPVKLVQQIEEKIDEWGLSKTNEDAFLAFRKHYNTNPNPLDLYVLSSFSYNYQFRFNNSMEFNNPFGRNRSHFSENMRNNLLNFVTKLQTLDATFTDNYFNEFDFSNLTSNDFIYLDPPYLITTGSYNDGKRGFSDWNNTSEMKLLNFMDYLNQHGIRFALSNVTEHKGKTNQLLKDWAYSRNLNVNYLDHNYNNSSHNSKSKGSQEVLITNYETKTFNLLNTK
|
An alpha subtype methylase that recognizes the double-stranded sequence 5'-GGATG-3' in one strand and 3'-CATCC-5' in the other, methylates A of both strands, and protects the DNA from cleavage by the StsI endonuclease. The 2 domains of the protein participate in modification of the two strands.
|
P29347
|
A5IYB2
|
TSAD_MYCAP
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Mycoplasmopsis
|
MKILGIETSHDDTSIAILENNKVVALETISQVDIFKEFGGTIPEISSREHVKNINLILEILIKKHDLSTIDYVAYTKEPGLVGTLQIGYLFANAVSLAYNKPIIPINHLAGHFYSCAIDHEINYPSLCLLVSGGHTQLMLINNPNDFQIIGQTLDDAVGEAFDKVSSKLQLGFPGGPIIDKIYKNYNGEFIKFTEPHAPGEYNFSFSGLKSQVINYYHNKIQRNEAIDINQIAASFQDCAVSYLINQTKKALRKYNVKSLVLAGGVSANSELRKRFLEISNIAIIPDLKYATDNGAMIASCAYQMLKEK
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
A5IYB2
|
Q9CH98
|
UVRC_LACLA
|
Excinuclease ABC subunit C
|
Lactococcus
|
MNQTIKAKLELLPDSPGCYLHKDKNGTVIYVGKAKNLKNRVRSYFHGSHNTKTELLVSEIEDLEWIVVGSNIESLVLEINLIQRYKPKYNIMLKDDKYYPFLKITNEKYPRLLVVRKVQKDGATYFGPYPDVKAANEVKRLLDRIFPFRKCGLHEKKVCFYFHIHQCLCPVVNHVDPQVFKDMTQEVKEFLTGSDKKIVNELEAKMMVSSDNMEFEQAAEYRDVIKAIGTLRTKQRVMNQDLKDRDVFGYYVDKGWMCVQVFFVRQGKLIQRDVNMFPYYNDAEEDFLTYIGQFYQDNNHMMPREIFIPQDIDKESVEAVVAASQEGNLLTKAQAKEVDAKVFTAKTLKFSDQKDVEQSIVKLDKELSAEKRLSSLLAKTQIVQPSRGEKKQLVNMATKNAQSQLQLKFDVAERDILKTTKAVENLGKILGIPKPVRIESFDNSNIMGTSPVSAMVVFIDGKPSKKDYRKYKIKTVVGADDYASMREVMTRRYSRALKEETALPDLIAMDGGAGQVNITKQVLKELGLSIPVAGMQKNDKHQTSELLFGDPLDVVPLSRQSQEFFLLTRIQDEVHRFAITFHRQLRGKNTFSSKLDGIVGLGPKRKQKLLTTFKNLKAIEEASVQEVAEADIPYEVAERVKTTLSGPIQENENWESLKDNVPLLEGKK
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
Q9CH98
|
Q980B5
|
RISB_SACS2
|
6,7-dimethyl-8-ribityllumazine synthase
|
Saccharolobus
|
MQEKSIRLGIVVAEFNYDITQLMLQKALSHARFLNVEVKVVIKVPGTFDMPLAIKKLLEKDFIDAVVTLGAVIKGETKHDELVASQTARKIVDLSTEFNKPVTLGIIGHGATHEQAVERIEEYATRAVEAAIKLVQRTRKLDELKEIKETVIIE
|
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
|
Q980B5
|
Q5B9N7
|
EIF3A_EMENI
|
Translation initiation factor eIF3, p110 subunit homolog
|
Aspergillus subgen. Nidulantes
|
MPPPPHIKPENVLKRAQELIAVGQAPAALTVLHEHATSKRTRSSPIASLEPVMLLFVELCVDLRKGKAAKDGLYQYKNIAQNSNVGTIEIVLKKFIELAEKKVTEAQAKADEIQSSLESAAPSSNVEDLEAIETPETILLATVSGEQSRDRTDRAVVTPWLKFLWETYRTVLEILKNNARLEIMYQTTALQAFQFCLKYTRKTEFRRLCELLRNHVQNAAKYSAQMHAINLSDPDTLQRHLDTRFQQLNVAVELELWQEAFRSIEDIHTLLSLSKRPAKNVMMANYYEKLARIFLVSENYLFHAAAWSRYYNLLRQSAVTLSTNQGSKKDHPSVTEADMTKAASFVLLSALAIPVISTSRSRGALIDVDEVRKNKNTRLTNLLGMLQSPTRAVLFRDALNKGLLKRVRPEIRELYNILEVDFHPLSICKKVTPILKKIGDDPEMEKYVVPLQQVILTRLFQQLSQVYESVELKFVYELAQFPDPFQITPSMIEKFIMNGCKKGDLAIRVDHISGVLTFDTDVFSSAKALHSGSAAGSAESELGSVQRLQNTPAEIARLQLTRLAKTLHVTCMYVDPSYNDSRLQAKQAALTRAAAGAAKEHEDTLERRVIIEKKKEAATDALQRKQKEEETRKRIRTQQLQEAEKQRLAEEQRERELKRIKDEQDRIRQQELKKQLEELKSGVKGIDLNEIDLEDLDANRLRAIKLAQLEKEKNELTERVRATGKRIDHLERAFRREELKHIAEDYEAQKKVDMEIYERQKAQTLAEAEAKHKEAVALKHRLSRLIPVFSSFRKEVSEKRHEEFEKRRKAAEREFEAKKKQRVKEVQERRRREKIERENAERAKREEEERIKREEEERAARDAERRRILAEEKAKREEERAKMDEIAAKQRQREEEAEARLRAKRAGLSEPPRTESEVRTAPRLNIAPRTSGGPSWRERQAAKEAAGGAAPEAPKAEPEPPRRTGGYVPPHARGGSDAAPPAGNRYVPPSQRSSQPPSRTQTPPTSSPKPEEPKPLASGTGGKWVPRWKQQQQNQ
|
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
|
Q5B9N7
|
O69754
|
PHZF_PSEAE
|
Phenazine/pyocyanine biosynthesis protein PhzF
|
Pseudomonas
|
MHRYVVIDAFASEPLQGNPVAVFFDCDDLSGERMQRMAREMNLSESTFVLRPQQDGDARIRIFTPVNELPFAGHPLLGTAIALGAETDKDRLFLETRMGTVPFALERQDGKVVACSMQQPIPTWEHFSRPAELLAALGLKGSTFPIEVYRNGPRHVFVGLESVAALSALHPDHRALCDFPDLAVNCFAGAGRHWRSRMFSPAYGVVEDAATGSAAGPLAIHLARHRQIPYGQQIEILQGVEIGRPSRMYARAEGAGERVSAVEVSGNGAAFAEGRAYL
|
Isomerase that catalyzes the condensation of two molecules of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine ring system. The final product is not yet known.
|
O69754
|
Q67LC0
|
FTSH1_SYMTH
|
ATP-dependent zinc metalloprotease FtsH 1
|
Symbiobacterium
|
MRWWAGAALLLAALLFGRPAAAMEAQPVAYSEFIQDVQARRVAYARITGQRLEAAYRDGTVRVVTLPPGEARLPLVLMQYGARVEFVRPADPIAFRTLLRFIPPLLILGAILWFTRRTAGGSGGLLTMEQSPARLYRVGEASVTLQDVAGLDEVKAELQEVIDFLREPERYRAMGARIPRGILLSGPPGTGKTLLARALAGEAGVPFFSASGSDFVELFAGTGAARVRALFDRARKAAPCIVFIDEIDALARRRGVGAGGGTEEREQTINQLLVEMDGFDSGEGVIVVAATNRPDVLDPAVLRPGRFDRHLTVDPPDRKGREQILAVHAREKRLSQAVALAEVARLTPGFTGADLANLLNEAALLAVRAGEREIGWPQVAMALERVTSGGPPRRVRAAAADRVRAAYHEAGHALAGLALRGSDRLVRVTILPHGRGLGHTLFRDQDEERYLHTRRDAFDRLTELLAGRAAEALVLGEVSAGAADDLERATGLAREMVTRWGMDADIGPLRLEHAVEGEESLRRADGAMRALVAAAERAARALLEARRSGLERLAAALLERERLEGPEVEALLELTPGEKPYIIVANSRGDEGNQ
|
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
|
Q67LC0
|
Q9NL39
|
MA14_PINMA
|
N14 matrix protein
|
Pinctada
|
MACTLRLTIAALVLLGICHLSRPVAAYQRCSRYWYSWLPYDIERDRYDDGYRKCCYCRNAWTPWQCREDEQFERMRCGSRYYTLCCYTDDDNGNGNGNGNGYGNGNGNGNGNNYLKYLFGGNGNGNGEYWEEYIDERYDK
|
May be specifically involved in the formation of the nacreous layer.
|
Q9NL39
|
Q95K73
|
ELOV4_MACFA
|
Very long chain 3-oxoacyl-CoA synthase 4
|
Macaca
|
MGLLDSEPGSVLNVVSTALNDTVEFYRWTWSIADKRVENWPLMQSPWPTLSISTLYLLFVWLGPKWMKDREPFQMRLVLIIYNFGMVLLNFFIFRELFMGSYNAGYSYICQSVDYSNNVNEVRIAAALWWYFVSKGVEYLDTVFFILRKKNNQVSFLHVYHHCTMFTLWWIGIKWVAGGQAFFGAQMNSFIHVIMYSYYGLAAFGPWIQKYLWWKRYLTMLQLVQFHVTIGHTALSLYTDCPFPKWMHWALIAYAISFIFLFLNFYIRTYKEPKKPKTGKTAMNGISANGVSKSEKQLVIENGKKQKNGKAKGD
|
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of very long chain saturated (VLC-SFA) and polyunsaturated (PUFA) fatty acids that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development.
|
Q95K73
|
Q5FVL7
|
KTU_RAT
|
Dynein assembly factor 2, axonemal
|
Rattus
|
MAKTAASSALEDLDLSGEEVQRLTSAFQDPEFRRMFSDYAAEITDPENRRRYEEEITALERERGVEVRFVHPEPGHVLRTSLDGEHRCFVNVCSNSLVGAPSSRPGPGRGGTAAGSHWSLPYSLAPGRQYAGRNGNRYTVYDVVFHPEALALARSHERFREMLDATALEAVEQQFGVRLDRRNAKTLKIKYKGTPEAAVLRTPLPEGVRAQPEGELPGLLPYPPYPYHYPAAAESTARSPASPAPKAVQRPEPTEPRCSVVQRHHVDLQDYRCSRDAAPSTVPHELVVTIELPLLRSAERAELEVKGKLLCLDSRNPDYRLRLSLPYPVDDGRGRAQYNKARRQLVVTLPVALAVARQDFSTTPEGPTAETGTDNIACTSAGDLAGAREESADSSGADHGRKSCVVAPDAGTAKAEGELVPEPEQDFGGDSVTPLGPGEGTTPENRSLLYSAFQSGDAESLAERSGVYGDLSVQTSEEQEGTCHDTSGSDMGGPGTESIKPLCPPLQCNQDEDSLTLLIQVPGIQPQSLHGDLSPFSYELCFSTQDSGYSFTLQFAPENKLSTKEPAISISLNNAVIVLAKSPESHGLWREWYWGLNKDSLEERLFIDEENVNEFLEEVVRSPLKPARSLSPPLIEVLQVTEEQIQIHAKLQECSDPDGLQGKEKGVKEECPLSEKENTEHSTTSTADSNSSVAVEGLKINTCGAVGLQQGCPDVPHVLSGKRLQSEAKMDPEFIRESSTAYSAEEKENIKEPVITKEKKIGGDHLSSLPNKTAVQNTHDFDTIKETNMQDGSVQIIKDHTTHCAFDFQNSLLYDLD
|
Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
|
Q5FVL7
|
P46136
|
YDDG_ECOLI
|
Aromatic amino acid exporter YddG
|
Escherichia
|
MTRQKATLIGLIAIVLWSTMVGLIRGVSEGLGPVGGAAAIYSLSGLLLIFTVGFPRIRQIPKGYLLAGSLLFVSYEICLALSLGYAATHHQAIEVGMVNYLWPSLTILFAILFNGQKTNWLIVPGLLLALVGVCWVLGGDNGLHYDEIINNITTSPLSYFLAFIGAFIWAAYCTVTNKYARGFNGITVFVLLTGASLWVYYFLTPQPEMIFSTPVMIKLISAAFTLGFAYAAWNVGILHGNVTIMAVGSYFTPVLSSALAAVLLSAPLSFSFWQGALMVCGGSLLCWLATRRG
|
Amino acid transporter with broad substrate specificity . Can transport various amino acids, including phenylalanine, tyrosine, tryptophan, L-threonine, L-methionine, L-lysine, L-glutamate, L-valine and L-isoleucine . Overexpression confers resistance to phenylalanine and increases export of phenylalanine, tyrosine and tryptophan .
|
P46136
|
P25264
|
MTC2_HERAU
|
Modification methylase HgiCII
|
Herpetosiphon
|
MKQFRFIDLFAGIGGFRLGLEAVGGICVGSAEIDQQAIKVYRQNWPTDRSEHNLGDITTLQQLPAHDLVVGGVPCQPWSIAGKNQAFDDPRGQLWADVIRLVRINQPKAFIFENVKGLIDPRNRLCLESILDSFKAEGYNVYYKLLNSFDYGVAQNRDRVFIIGIQQKLGVPDFSFPEYSESEQRLYDILDNLQTPSIIPESLPIQRNLFGERIEVGFNKLTPRGAFNDFFILNDIRNGPTSIHSWEIYATTEREKQICTTIMRNRGNPRYGDCDGNPMSYQDIADLVVDLAESELQVLIQKRILRQYEDGKYEFFNRRLSGGIDGTYRIFLPHARFFGRLTARGMHDEIAEISVSGATAEAYKQNFIQQILIPKRHRPITVNEAARIQGFPATFKFHSNQSANFRLIGNSVAPPVIMALGKALPNDHLFEPELCEV
|
A methylase that recognizes the double-stranded sequence 5'-GGWCC-3', methylates C-? on both strands and protects the DNA from cleavage by the HgiCII endonuclease.
|
P25264
|
Q3J376
|
PSTB_CERS4
|
Phosphate-transporting ATPase
|
Cereibacter
|
MDDIRYADRIVSADEVKIAARKAQVFYGSNHALRDVDVDILGKTVTAFIGPSGCGKSTFLRCLNRMNDTIPGCRVEGKITLDGQDIYDTRVDPVQLRAKVGMVFQKPNPFPKSIYDNVAYGPRIHGLARSKAEIDEIVEGALRRAALWNEAKDRLSSPGTGLSGGQQQRLCIARAIATSPEVLLMDEPCSALDPIATAQIEELIDELRAQFSVVIVTHSMQQAARVSQRTAFFHLGRLVEYGETGQIFTNPRDPRTESYISGRIG
|
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
|
Q3J376
|
Q56225
|
NQO10_THET8
|
NDH-1 subunit 10
|
Thermus
|
MSLLEGLALFLLLLSGVLVVTLRNAIHAALALILNFLVLAGVYVALDARFLGFIQVIVYAGAIVVLFLFVIMLLFAAQGEIGFDPLVRSRPLAALLALGVAGILAAGLWGLDLAFTQDLKGGLPQALGPLLYGDWLFVLLAVGFLLMAATVVAVALVEPGKASRAKEAEKREEVAR
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.
|
Q56225
|
O25690
|
KHSE_HELPY
|
Homoserine kinase
|
Helicobacter
|
MVVSVPATSANLGPGFDCLGLSLNLRNRFFIEPSSFHAVKLVGEGEGIPKFLTNNIFTKVFYEILKKHGNDGSFKFLLHNKVPITRGMGSSSAMIVGAVASAFAFLGFDFDRENIVNTALIYENHPDNITPAVFGGYNAAFVEKKKVISLKTKIPSFLKAVMVIPNRAISTKQSRHLLPKRYSVQESVFNLSHASLMTMAIVQGKWDLLRCCSKDRMHQYKRMQTYPVLFAIQKIALENNALMSTLSGSGSSFFNMCYEEDAPKLKQVLSKKFPKFRVAVLDFDNDGVLIEKD
|
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
|
O25690
|
A7N1Z7
|
TAL_VIBC1
|
Transaldolase
|
Vibrio
|
MSNKLEQLRKLTTVVADTGEIDAIKKYQPEDATTNPSLILKAAQIEEYAPLIDASIEYAKAQSNDKAQQVQDTCDMLAVNIGKEILKTIPGRISTEVDARLSYDTEGSVAKARQLVKMYNDAGITNDRILIKLASTWEGIRAAEILEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRIMDWYKAKEGRDFEASEDPGVISVTDIYNYYKDYGYNTVVMGASFRNIGEILELAGCDRLTIAPALLAELEAAEGEVVEKLVDSKGSKERPAPMSHAEFLWEHNLDAMAVEKVAEGIRNFAVDQGKLEDMIAAKL
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
A7N1Z7
|
Subsets and Splits
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